Marielle Aulikki Hegetschweiler

Marielle Aulikki Hegetschweiler

Assistant Professor, Chemistry and Biochemistry-Sci
Member of the Graduate Faculty
Primary Department
Department Affiliations

Work Summary

Most proteins need to attain a 3D structure to function properly. They are synthesized as unfolded chains and must fold into the right structure. Failure in this process can lead to protein misfolding diseases such as Alzheimer’s disease, Huntington's disease, Parkinson's disease, Creutzfeld-Jakob disease, or cystic Fibrosis. Chaperones play a crucial role in maintaining protein homeostasis, but the mechanism of how they work is not fully understood. In our group, we focus on Hsp60 and its obligate substrates, including Ab (the Alzheimer's peptide), malate dehydrogenase, and superoxide dismutase. Through the use of solution-state NMR, cryo-electron microscopy, and various other biochemical assays, we investigate the mechanism by which Hsp60 assists in protein folding and prevents the toxic aggregation of Ab.

Research Interest

The objective of our group is to elucidate the functioning of chaperones, with a specific focus on Hsp60. We are investigating the mechanism by which Hsp60 facilitates protein folding and prevents protein aggregation. This research is particularly significant in the context of Alzheimer's disease and specific types of cancer. To accomplish this, we employ various biochemical assays, with an emphasis on solution-state NMR and cryo-electron microscopy. Our research involves the examination of structures and the quantitative analysis of interactions.